Enzyme Lab Report

Enzymes are biological catalysts, which means it decreases activation energy in reactions. The lower activation energy in a reaction, the faster the reaction rate. Many enzymes alter their shape when they bind to the activation site. This is called induced fit, meaning for the enzyme to work to its full potential it has to change shape to binding substrate. The location of enzyme’s activation site is on the surface of the enzyme, where the binding of substrates take place. Enzyme activity can be influenced by a variety of environmental factors. If the concentration of enzyme is low, and there is a great deal of substrate, then increasing enzyme concentration results in more molecules available to convert substrates to products. Thus, increasing enzyme concentration can increase reaction rate. If substrate concentrations are low, and many of the existing enzymes are idle because of a lack of substrate, then adding enzyme will have no effect on reaction rate. Enzyme concentration affects the enzyme activity, because the more enzyme concentration the faster the reaction rate, until it hits it’s limiting factor. When substrate concentration is increased, it also increases rate of reaction. Temperature plays an important

Enzyme catalysis is dependant upon factors such as concentration of enzyme and substrate, temperature and pH. These factors determine the rate of reaction, and an increase in temperature or pH above the optimum will

From Figure 5, Vmax = 0.0172 and Km = 0.3144. At ½ Vmax (Figure 4), the rate of reaction increases steadily with an increase in substrate concentration. At this point, the rate of product formation is partially limited by substrate availability. As the curve approaches Vmax, the enzyme catalyzed saturation increases. In effect, the enzyme activity increases the rate of product formation up to a point whereby the reaction rate remains constant as more substrate is added (saturation).

pH - Enzymes also have an optimum pH level. The pH of a solution affects the enzyme's secondary and tertiary structures. These bonds make the shape of an enzyme's active site. So, if these bonds are broken, the shape of the active site changes and is distorted. If there is no active site, there is no reaction resulting in no products. If the enzyme is put in a pH that is very different from the optimum pH, it can cause the enzyme to denature.

PH can affect the way fermentation occurs due to the irregularity of the acidity or alkalinity within the glucose solution. This is an enzyme-based reaction that is susceptible to pH. The aim of this experiment was to determine how pH affects the yeast fermentation rate by performing the experiment numerous times with a different pH of glucose solution which included pH 3, 5, 7, 9, 11. The hypothesis was ‘If the pH is lower than the neutral point then the fermentation reaction will occur faster?’ The experiment conducted was to measure the amount of C02 produced by the yeast going into fermentation, however varying the pH of glucose solution by using different pHs . To test this every 5 minutes the volume of gas in the test tube was observed and recorded until a period of 30 minutes had been. The end results

Drop the yeast sphere into the graduated cylinder. As soon as the sphere touches the surface of the hydrogen peroxide, start the timer. Each person should be responsible for a concentration.

Background and Introduction: Enzymes are proteins that process substrates, which is the chemical molecule that enzymes work on to make products. Enzyme purpose is to increase the rate of activity and speed up chemical reaction in a form of biological catalysts. The enzymes specialize in lowering the activation energy to start the process. Enzymes are very specific in their process, each substrate is designed to fit with a specific substrate and the enzyme and substrate link at the active site. The binding of a substrate to the active site of an enzyme is a very specific interaction. Active sites are clefts or grooves on the surface of an enzyme, usually composed of amino acids from different parts of the polypeptide chain that are brought together in the tertiary structure of the folded protein. Substrates initially bind to the active site by noncovalent interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions. Once a substrate is bound to the active site of an enzyme, multiple mechanisms can accelerate its conversion to the product of the reaction. But sometimes, these enzymes fail or succeed to increase the rate of action because of various factors that limit the action. These factors can be known as temperature, acidity levels (pH), enzyme and/or substrate concentration, etc. In this experiment, it will be tested how much of an effect

1) The substrate for this procedure was hydrogen peroxide. The enzyme used (contained in the yeast) would have most likely been catalase.

To improve the results from the experiment buffer solutions that were not whole pHs could have been used e.g. pH 4.5, 5.5 etc. This would have provided more reliable results as a wider range of results would have been produced. Using pHs with decimals would also help to more accurately determine the optimum pH as the optimum may have been above or below the pH stated in the hypothesis; 8. In this experiment however the optimum is taken at 8 because the graph does not rise again.

The first experiment begun by filling a 600-ml beaker, almost to the top, with water. Next, a 10-ml graduated cylinder was filled to the top with water. Once water was added to the beaker and graduated cylinder, a thumb was placed over the top of the graduated cylinder. This would ensure that no water was let out and no bubbles were let into the graduated cylinder. Next, it was turned upside down and fully submerged into the beaker. Then, a U-shaped glass tube was attained. The short end of the glass tube was placed into the beaker with the tip inside of the graduated cylinder. Next, a 50-ml Erlenmeyer flask was received. After, 10-ml of substrate concentration and 10-ml of catalase/buffer solution were placed into the flask. A rubber stopper was then placed on the opening of the flask. After adding these, the flask was held at the neck and spun softly

Changes in pH also alter an enzyme’s shape. Different enzymes work best at different pH values. The optimum pH for an enzyme depends on where it normally works. For example, intestinal enzymes have an optimum pH of about 7.5 whereas enzymes in the stomach have an optimum pH of about 2.

What does the changes in the amount of substrate on an enzyme’s reaction effect on?

However, the rate of reaction only increases for a certain period of time until there is lesser substrate molecules than the enzyme molecules. The increase of enzyme concentration does not have effect if there are lesser substrate molecules than enzyme molecules initially.

“Enzymes are proteins that have catalytic functions” [1], “that speed up or slow down reactions”[2], “indispensable to maintenance and activity of life”[1]. They are each very specific, and will only work when a particular substrate fits in their active site. An active site is “a region on the surface of an enzyme where the substrate binds, and where the reaction occurs”[2].

As an enzyme-catalyzed reaction may be the main reason for a reaction to occur faster, many factors can